ID A0A084A570_9GAMM Unreviewed; 360 AA.
AC A0A084A570;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
DE EC=2.7.8.33 {ECO:0000256|HAMAP-Rule:MF_02030};
DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
DE AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
GN Name=wecA {ECO:0000256|HAMAP-Rule:MF_02030,
GN ECO:0000313|EMBL:KEY60449.1};
GN ORFNames=SRDD_06110 {ECO:0000313|EMBL:KEY60449.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY60449.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY60449.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY60449.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
CC -!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from
CC UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P),
CC yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55).
CC {ECO:0000256|HAMAP-Rule:MF_02030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-
CC undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:28090,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392,
CC ChEBI:CHEBI:62959; EC=2.7.8.33; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02030,
CC ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02030};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02030}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02030}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02030}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02030}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02030}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEY60449.1}.
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DR EMBL; AYKS02000017; KEY60449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084A570; -.
DR STRING; 1410619.SRDD_06110; -.
DR eggNOG; COG0472; Bacteria.
DR UniPathway; UPA00281; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000017810; Unassembled WGS sequence.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06853; GT_WecA_like; 1.
DR HAMAP; MF_02030; WecA_Gammaproteo; 1.
DR InterPro; IPR012750; ECA_WecA-rel.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR NCBIfam; TIGR02380; ECA_wecA; 1.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02030};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02030};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02030};
KW Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW ECO:0000256|HAMAP-Rule:MF_02030};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02030, ECO:0000256|PIRSR:PIRSR600715-
KW 1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_02030};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02030};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02030};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02030};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02030}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 44..60
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 66..84
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 156..174
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 289..307
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT TRANSMEM 313..332
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 360 AA; 40289 MW; 4EFFE039469582E3 CRC64;
MSTEILFVFL FSLAFLFVAR KVAKRIGLVD KPNYRKRHQG LIPLVGGISV YAGLCFAFLI
TDVPIVHSKL YLACAGVLVF VGALDDRFDI SVKIRATVQA LVGVAMMLFA DLYLHSLGQV
FGNWEMLLGP FGYLVTLFAV WAAINAFNMV DGIDGLLGGL SCVSFGAMGI LLYQSGNNEL
AFWCFAMLAA IVPYILLNLG VLGRRYKVFM GDAGSTLIGF TAIWLLLQSS QGENHPIRPV
TALWIIAIPL MDMIAIMYRR LRKGMSPFSP DRQHIHHLIM RAGFTPRQAF VLITLAAAIL
AAIGIIGERL SFIPEWVMLV LFLLAFFFYG YCIKRAWRVA RYIKRIKRRI RNSMHNKQVP
//
